This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


208l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:208l.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:208l.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_208l| PDB=208l | SCENE= }}
{{STRUCTURE_208l| PDB=208l | SCENE= }}
-
'''MUTANT HUMAN LYSOZYME C77A'''
+
===MUTANT HUMAN LYSOZYME C77A===
-
==Overview==
+
<!--
-
We previously reported that protein disulfide isomerase (PDI) can dissociate the glutathione molecule in vitro from the mutant human lysozyme (hLZM) C77A-a, which is modified with glutathione at Cys95; however, it seems structurally difficult for PDI to attack either the disulfide bond or the side chain of the cysteine residue of a mixed disulfide. To investigate the function of PDI, we introduced several glutathione and cysteine derivatives at Cys95, instead of the glutathione of C77A-a. Using thiol compounds modified by 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB), we could easily modify the free thiol group of C77A-b (C77A with no glutathionylation), without denaturation. For all of the modifications we tested, a negative correlation was found between the initial rate and the acceleration ratio of the reductive cleavage of mixed disulfides with PDI. A mutant PDI (hPDIM), which has no thiol-disulfide exchange activity, suppressed the reductive cleavage of the mixed disulfide of C77A-a with hPDI, suggesting that hPDI non-covalently interacted with the substrates. Taking account of the results of the structural analysis, we conclude that one of the functions of PDI in vivo lies in relaxing the structure around the disulfide bond, as well as in exchanging the thiol-disulfide bonds.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8902616}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8902616 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8902616}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Mutant human lysozyme]]
[[Category: Mutant human lysozyme]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:18:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:10:27 2008''

Revision as of 04:10, 28 July 2008

Image:208l.png

Template:STRUCTURE 208l

MUTANT HUMAN LYSOZYME C77A

Template:ABSTRACT PUBMED 8902616

About this Structure

208L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A role of PDI in the reductive cleavage of mixed disulfides., Nakamura S, Matsushima M, Song H, Kikuchi M, J Biochem. 1996 Sep;120(3):525-30. PMID:8902616

Page seeded by OCA on Mon Jul 28 07:10:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/208l"
Personal tools